氰化物与氧化型细胞色素c氧化酶结合的动力学研究。
Kinetic studies on the binding of cyanide to oxygenated cytochrome c oxidase.
作者信息
Brittain T, Greenwood C
出版信息
Biochem J. 1976 May 1;155(2):453-5. doi: 10.1042/bj1550453.
Abstract
The reaction of cyanide with oxygenated cytochrome c oxidase was followed by means of flow-flash techniques. The oxygenated form, produced after photolysis of the partially reduced CO complex in the presence of cyanide and O2, shows cyanide-binding properties distinct from those of both the oxidized and the reduced forms of the protein. The binding is a single process (k = 22M-1-S-1) linearly dependent on cyanide concentration to as high as 75 mM. It is suggested that the oxygenated form is a conformational variant of the oxidized protein.
摘要
通过流动闪光技术跟踪氰化物与氧化型细胞色素c氧化酶的反应。在氰化物和氧气存在下，部分还原的一氧化碳复合物光解后产生的氧化形式，其氰化物结合特性与蛋白质的氧化形式和还原形式均不同。这种结合是一个单一过程（k = 22M⁻¹·s⁻¹），与氰化物浓度呈线性相关，最高可达75 mM。有人认为氧化形式是氧化型蛋白质的一种构象变体。
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